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1
Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN
Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN
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Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN

Yoshimoto, Francis K. ; Gonzalez, Eric ; Auchus, Richard J. ; Guengerich, F. Peter

The Journal of biological chemistry, 2016-08, Vol.291 (33), p.17143-17164 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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2
Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome
Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome
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Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome

Sugishima, Masakazu ; Wada, Kei ; Fukuyama, Keiichi ; Yamamoto, Ken

The Journal of biological chemistry, 2020-01, Vol.295 (3), p.771-782 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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3
A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis
A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis
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A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis

Glasgow, Evan M. ; Kemna, Elias I. ; Bingman, Craig A. ; Ing, Nicole ; Deng, Kai ; Bianchetti, Christopher M. ; Takasuka, Taichi E. ; Northen, Trent R. ; Fox, Brian G.

The Journal of biological chemistry, 2020-10, Vol.295 (51), p.17752-17769 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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4
Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance
Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance
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Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance

Fahrig-Kamarauskait≑, Jūrate˙ ; Würth-Roderer, Kathrin ; Thorbjørnsrud, Helen V. ; Mailand, Susanne ; Krengel, Ute ; Kast, Peter

The Journal of biological chemistry, 2020-10, Vol.295 (51), p.17514-17534 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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5
Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation
Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation
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Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation

Nandi, Suparno ; Razzaghi, Mortezaali ; Srivastava, Dhiraj ; Dey, Mishtu

The Journal of biological chemistry, 2020-09, Vol.295 (51), p.17425-17440 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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6
Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164
Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164
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Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164

Armstrong, Zachary ; Davies, Gideon J.

The Journal of biological chemistry, 2019-12, Vol.295 (13), p.4316-4326 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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7
Enzymology and significance of protein histidine methylation
Enzymology and significance of protein histidine methylation
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Enzymology and significance of protein histidine methylation

Jakobsson, Magnus E.

The Journal of biological chemistry, 2021-10, Vol.297 (4), p.101130-101130, Article 101130 [Periódico revisado por pares]

Elsevier Inc

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8
The Reductive Half-reaction of Xanthine Dehydrogenase from Rhodobacter capsulatus: THE ROLE OF GLU
The Reductive Half-reaction of Xanthine Dehydrogenase from Rhodobacter capsulatus: THE ROLE OF GLU
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The Reductive Half-reaction of Xanthine Dehydrogenase from Rhodobacter capsulatus: THE ROLE OF GLU

Hall, James ; Reschke, Stefan ; Cao, Hongnan ; Leimkühler, Silke ; Hille, Russ

The Journal of biological chemistry, 2014-09, Vol.289 (46), p.32121-32130 [Periódico revisado por pares]

9650 Rockville Pike, Bethesda, MD 20814, U.S.A: American Society for Biochemistry and Molecular Biology

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9
Revealing the Mechanism of Action of the Industrially Important Enzyme Nitrile Hydratase♦: A Protein-derived Oxygen Is the Source of the Amide Oxygen of Nitrile Hydratases
Revealing the Mechanism of Action of the Industrially Important Enzyme Nitrile Hydratase♦: A Protein-derived Oxygen Is the Source of the Amide Oxygen of Nitrile Hydratases
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Revealing the Mechanism of Action of the Industrially Important Enzyme Nitrile Hydratase♦: A Protein-derived Oxygen Is the Source of the Amide Oxygen of Nitrile Hydratases

The Journal of biological chemistry, 2016-04, Vol.291 (15), p.7830-7830 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: Elsevier Inc

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10
Structure and Catalytic Mechanism of a Key Drug Target in the Pathogen Pseudomonas aeruginosa: PqsBC, a Condensing Enzyme in the Biosynthesis of the
Structure and Catalytic Mechanism of a Key Drug Target in the Pathogen Pseudomonas aeruginosa: PqsBC, a Condensing Enzyme in the Biosynthesis of the
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Structure and Catalytic Mechanism of a Key Drug Target in the Pathogen Pseudomonas aeruginosa: PqsBC, a Condensing Enzyme in the Biosynthesis of the

The Journal of biological chemistry, 2016-03, Vol.291 (13), p.6625-6625 [Periódico revisado por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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